Phosphorylated Protein Levels in Animal-Sourced Food Muscles Based on Fe 3+ and UV/Vis Spectrometry

Protein phosphorylation, a post-translational modification of proteins, is important in biological regulation. The quantity of phosphorylated proteins is a key requirement for the quality change of animal muscle foods. In the present study, a new approach to quantify phosphorylated proteins and/or p...

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Bibliographic Details
Published in:ACS omega 2022-03, Vol.7 (8), p.6560-6567
Main Authors: Cui, Rong, Shao, Mingke, Bi, Hongyan
Format: Article
Language:English
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Summary:Protein phosphorylation, a post-translational modification of proteins, is important in biological regulation. The quantity of phosphorylated proteins is a key requirement for the quality change of animal muscle foods. In the present study, a new approach to quantify phosphorylated proteins and/or peptides was developed based on ferric ions (Fe ) and UV/vis spectrometry. This method is proved to be ultra-effective in discriminating phosphopeptides and non-phosphopeptides with the assistance of Fe . The protocol of extracting proteins with 0.1% trifluoroacetic acid (TFA) solution from animal muscle samples coupled with Fe was verified by using an artificial mixture of peptides with different phosphorylation sites and was successfully used to characterize the phosphorylation quantity in the samples via UV/vis spectrometry. A peptide with one phosphorylated site was taken as a reference standard and successfully utilized for the absolute quantification of phosphorylated proteins in caprine muscles during frozen storage and in fish muscle food samples. This present study paves a new way for the evaluation of phosphorylated protein quantitative levels in bio-samples.
ISSN:2470-1343
2470-1343
DOI:10.1021/acsomega.1c05641